KT5AA_XENLA
ID KT5AA_XENLA Reviewed; 335 AA.
AC Q08AY6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=N-lysine methyltransferase KMT5A-A {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Histone-lysine N-methyltransferase KMT5A-A;
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Lysine-specific methylase 5A-A {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=SET domain-containing protein 8-A;
GN Name=kmt5a-a {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=setd8-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine N-methyltransferase that monomethylates both
CC histones and non-histone proteins. Specifically monomethylates 'Lys-20'
CC of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and
CC represents a specific tag for epigenetic transcriptional repression.
CC Mainly functions in euchromatin regions, thereby playing a central role
CC in the silencing of euchromatic genes. Required for cell proliferation,
CC probably by contributing to the maintenance of proper higher-order
CC structure of DNA during mitosis. Involved in chromosome condensation
CC and proper cytokinesis. {ECO:0000250|UniProtKB:Q9NQR1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000250|UniProtKB:Q9NQR1, ECO:0000255|PROSITE-
CC ProRule:PRU00904};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q9NQR1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQR1}.
CC Chromosome {ECO:0000250|UniProtKB:Q9NQR1}. Note=Specifically localizes
CC to mitotic chromosomes. Associates with silent chromatin on euchromatic
CC arms (By similarity). {ECO:0000250|UniProtKB:Q9NQR1}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00904}.
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DR EMBL; BC124952; AAI24953.1; -; mRNA.
DR RefSeq; NP_001121300.1; NM_001127828.1.
DR AlphaFoldDB; Q08AY6; -.
DR SMR; Q08AY6; -.
DR DNASU; 100158384; -.
DR GeneID; 100158384; -.
DR KEGG; xla:100158384; -.
DR CTD; 100158384; -.
DR Xenbase; XB-GENE-865841; kmt5a.S.
DR OMA; THHEAKC; -.
DR OrthoDB; 1460495at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 100158384; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW Methyltransferase; Mitosis; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..335
FT /note="N-lysine methyltransferase KMT5A-A"
FT /id="PRO_0000317000"
FT DOMAIN 199..320
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 281..282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
SQ SEQUENCE 335 AA; 38092 MW; 4300EFC00C1210A9 CRC64;
MGRGKKMSKP GDGRSGDVSD TGRNGGTNEN HPKTNGEVVH CGQAKIYSYM SPTKSPSARP
PLQEENSVTH HESKCLGKPS TETRKKAEVE KKKILSTELS VKPSEQRETE CNSIGEFLEP
KLELNDVQRN LALPPEDKLQ SQKMVKNKPL RKKTQRQKSP NRKLTDYYPV RRSSRKNKTE
IESEEKKRID ELIQTGKEEG IKMHMITGKG RGVIATRDFQ RGEFVVEYHG DLIEITDAKR
REASYAQDSA TGCYMYYFQY LNTSYCIDAT RETGRLGRLI NHSKSGNCHT KLHNINNVPH
LILVASRDIN VGEELLYDYG DRRKSSIDAH PWLKN
